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PDBsum entry 3gcb
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References listed in PDB file
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Key reference
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Title
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The unusual active site of gal6/bleomycin hydrolase can act as a carboxypeptidase, Aminopeptidase, And peptide ligase.
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Authors
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W.Zheng,
S.A.Johnston,
L.Joshua-Tor.
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Ref.
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Cell, 1998,
93,
103-109.
[DOI no: ]
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PubMed id
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Abstract
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The Gal6 protease is in a class of cysteine peptidases identified by their
ability to inactivate the anti-cancer drug bleomycin. The protein forms a barrel
structure with the active sites embedded in a channel as in the proteasome. In
Gal6 the C termini lie in the active site clefts. We show that Gal6 acts as a
carboxypeptidase on its C terminus to convert itself to an aminopeptidase and
peptide ligase. The substrate specificity of the peptidase activity is
determined by the position of the C terminus of Gal6 rather than the sequence of
the substrate. We propose a model to explain these diverse activities and Gal6's
singular ability to inactivate bleomycin.
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Figure 3.
Figure 3. G450A Has a Different Processing Pattern from the
Wild-Type ProteinAn electrospray mass spectrometry shows G450A
protein cleaving either one or three residues of the C terminus.
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Figure 6.
Figure 6. Possible Mechanism of Bleomycin Hydrolysis by
Bleomycin Hydrolase
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1998,
93,
103-109)
copyright 1998.
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Secondary reference #1
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Title
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Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6.
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Authors
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L.Joshua-Tor,
H.E.Xu,
S.A.Johnston,
D.C.Rees.
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Ref.
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Science, 1995,
269,
945-950.
[DOI no: ]
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PubMed id
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